Wachtel E J, Sverbilova T, McCubbin W D, Kay C M
Department of Polymer Research, Weizmann Institute of Science, Rehovot, Israel.
Biochem J. 1989 Aug 1;261(3):1043-6. doi: 10.1042/bj2611043.
The solution structure of troponin C from turkey skeletal muscle was studied at low pH by small-angle X-ray-scattering. We find that troponin C at pH 5.3 in the presence of Mg2+ has a triaxial radius of gyration and maximum dimension comparable with those of the crystallized protein. However, the relative disposition of domains is more similar to that found for the highly homologous rabbit protein in solution at pH 7.4.
通过小角X射线散射研究了火鸡骨骼肌肌钙蛋白C在低pH值下的溶液结构。我们发现，在Mg2+存在下，pH 5.3的肌钙蛋白C具有与结晶蛋白相当的三轴回转半径和最大尺寸。然而，结构域的相对排列与在pH 7.4溶液中高度同源的兔蛋白更为相似。
